Aliases for HSPD1 Gene
External Ids for HSPD1 Gene
Previous HGNC Symbols for HSPD1 Gene
Previous GeneCards Identifiers for HSPD1 Gene
This gene encodes a member of the chaperonin family. The encoded mitochondrial protein may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. This gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Several pseudogenes have been associated with this gene. Two transcript variants encoding the same protein have been identified for this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13. [provided by RefSeq, Jun 2010]
GeneCards Summary for HSPD1 Gene
HSPD1 (Heat Shock Protein Family D (Hsp60) Member 1) is a Protein Coding gene. Diseases associated with HSPD1 include Leukodystrophy, Hypomyelinating, 4 and Spastic Paraplegia 13, Autosomal Dominant. Among its related pathways are Validated targets of C-MYC transcriptional activation and Tuberculosis. GO annotations related to this gene include poly(A) RNA binding and ATPase activity.
UniProtKB/Swiss-Prot for HSPD1 Gene
Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:1346131, PubMed:11422376). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).